ArticleVirology journal2010
Human immunodeficiency virus type 1 Vpr: oligomerization is an essential feature for its incorporation into virus particles.
Article in Virology journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- HIV-1 Vpr Functions in Primary CD4Viruses · 2024Review
- HIV-1 Gag Recruits Oligomeric Vpr via Two Binding Sites in p6, but Both Mature p6 and Vpr Are Rapidly Lost upon Target Cell Entry.Journal of virology · 2021Article
- Article
- Review
- HIV-1 Integrase-Targeted Short Peptides Derived from a Viral Protein R Sequence.Molecules (Basel, Switzerland) · 2018Article
- The ClusPro web server for protein-protein docking.Nature protocols · 2017Article
- Specific amino acids in HIV-1 Vpr are significantly associated with differences in patient neurocognitive status.Journal of neurovirology · 2017Article
- The HIV-1 Vpr Protein: A Multifaceted Target for Therapeutic Intervention.International journal of molecular sciences · 2017Review
- Virion encapsidated HIV-1 Vpr induces NFAT to prime non-activated T cells for productive infection.Open biology · 2016Article
- Functional antagonism of TMPRSS2-ERG splice variants in prostate cancer.Genes & cancer · 2014Article
- Human immunodeficiency virus type 1 Vpr polymorphisms associated with progressor and nonprogressor individuals alter Vpr-associated functions.The Journal of general virology · 2014Article
- The phosphorylation of HIV-1 Gag by atypical protein kinase C facilitates viral infectivity by promoting Vpr incorporation into virions.Retrovirology · 2014Article
- The HIVToolbox 2 web system integrates sequence, structure, function and mutation analysis.PloS one · 2014Article
- HIV-1 Vpr-a still "enigmatic multitasker".Frontiers in microbiology · 2014Review
- DOT2: Macromolecular docking with improved biophysical models.Journal of computational chemistry · 2013Article
- Exosomes derived from HIV-1-infected cells contain trans-activation response element RNA.The Journal of biological chemistry · 2013Article
- Development of a robust cell-based high-throughput screening assay to identify targets of HIV-1 viral protein R dimerization.Drug design, development and therapy · 2013Article
- Delineating HIV-associated neurocognitive disorders using transgenic models: the neuropathogenic actions of Vpr.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2012Review
- Article
- Human immunodeficiency virus viral protein R as an extracellular protein in neuropathogenesis.Advances in virus research · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
HIV-1 Vpr, a nonstructural viral protein associated with virus particles, has a positive role in the efficient transport of PIC into the nucleus of non-dividing target cells and enhances virus replication in primary T cells. Vpr is a 96 amino acid protein and the structure by NMR shows three helical domains. Vpr has been shown to exist as dimers and higher order oligomers. Considering the multifunctional nature of Vpr, the contribution of distinct helical domains to the dimer/oligomer structure of Vpr and the relevance of this feature to its functions are not clear. To address this, we have utilized molecular modeling approaches to identify putative models of oligomerization. The predicted interface residues were subjected to site-directed mutagenesis and evaluated their role in intermolecular interaction and virion incorporation. The interaction between Vpr molecules was monitored by Bimolecular Fluorescence complementation (BiFC) method. The results show that Vpr forms oligomers in live cells and residues in helical domains play critical roles in oligomerization. Interestingly, Vpr molecules defective in oligomerization also fail to incorporate into the virus particles. Based on the data, we suggest that oligomerization of Vpr is essential for virion incorporation property and may also have a role in the events associated with virus infection.
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Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.